ASNA_UREU1
ID ASNA_UREU1 Reviewed; 329 AA.
AC B5ZBH5;
DT 14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT 25-NOV-2008, sequence version 1.
DT 25-MAY-2022, entry version 65.
DE RecName: Full=Aspartate--ammonia ligase {ECO:0000255|HAMAP-Rule:MF_00555};
DE EC=6.3.1.1 {ECO:0000255|HAMAP-Rule:MF_00555};
DE AltName: Full=Asparagine synthetase A {ECO:0000255|HAMAP-Rule:MF_00555};
GN Name=asnA {ECO:0000255|HAMAP-Rule:MF_00555}; OrderedLocusNames=UUR10_0372;
OS Ureaplasma urealyticum serovar 10 (strain ATCC 33699 / Western).
OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Ureaplasma.
OX NCBI_TaxID=565575;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 33699 / Western;
RA Shrivastava S., Methe B.A., Glass J., White K., Duffy L.B.;
RT "Genome sequence of Ureaplasma urealyticum serovar 10 ATCC-33699.";
RL Submitted (OCT-2008) to the EMBL/GenBank/DDBJ databases.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + L-aspartate + NH4(+) = AMP + diphosphate + H(+) + L-
CC asparagine; Xref=Rhea:RHEA:11372, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:28938, ChEBI:CHEBI:29991, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:33019, ChEBI:CHEBI:58048, ChEBI:CHEBI:456215; EC=6.3.1.1;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_00555};
CC -!- PATHWAY: Amino-acid biosynthesis; L-asparagine biosynthesis; L-
CC asparagine from L-aspartate (ammonia route): step 1/1.
CC {ECO:0000255|HAMAP-Rule:MF_00555}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00555}.
CC -!- SIMILARITY: Belongs to the class-II aminoacyl-tRNA synthetase family.
CC AsnA subfamily. {ECO:0000255|HAMAP-Rule:MF_00555}.
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DR EMBL; CP001184; ACI60345.1; -; Genomic_DNA.
DR RefSeq; WP_004026193.1; NC_011374.1.
DR AlphaFoldDB; B5ZBH5; -.
DR SMR; B5ZBH5; -.
DR STRING; 565575.UUR10_0372; -.
DR EnsemblBacteria; ACI60345; ACI60345; UUR10_0372.
DR GeneID; 45015919; -.
DR KEGG; uue:UUR10_0372; -.
DR eggNOG; COG2502; Bacteria.
DR HOGENOM; CLU_071543_0_0_14; -.
DR OMA; QSRICMF; -.
DR OrthoDB; 487853at2; -.
DR UniPathway; UPA00134; UER00194.
DR Proteomes; UP000002018; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0004071; F:aspartate-ammonia ligase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0070981; P:L-asparagine biosynthetic process; IEA:UniProtKB-UniPathway.
DR Gene3D; 3.30.930.10; -; 1.
DR HAMAP; MF_00555; AsnA; 1.
DR InterPro; IPR006195; aa-tRNA-synth_II.
DR InterPro; IPR045864; aa-tRNA-synth_II/BPL/LPL.
DR InterPro; IPR004618; AsnA.
DR PANTHER; PTHR30073; PTHR30073; 1.
DR Pfam; PF03590; AsnA; 1.
DR PIRSF; PIRSF001555; Asp_ammon_ligase; 1.
DR SUPFAM; SSF55681; SSF55681; 1.
DR PROSITE; PS50862; AA_TRNA_LIGASE_II; 1.
PE 3: Inferred from homology;
KW Amino-acid biosynthesis; Asparagine biosynthesis; ATP-binding; Cytoplasm;
KW Ligase; Nucleotide-binding.
FT CHAIN 1..329
FT /note="Aspartate--ammonia ligase"
FT /id="PRO_1000129137"
SQ SEQUENCE 329 AA; 38277 MW; E52EC9D06DCD013E CRC64;
MGQLQKAKIN QTQKAIVEIK NRFQKYFAKN LNLSRVTAPL FVEGQSGLND HLDHKQKAVS
FYAKKLNKTL EIVQSLAKWK RLALLDYGFS LYEGLYTDMN AIRADDDIDE IHSIYVDQWD
WEILINKQDC TLDFLKSIVN KIYSTIKTVQ LEIDQLYNPK QIILPDSITF IGSQELEDLY
PHLTPSQREY EFAKMHQAIF IYQIGYPLKS GYIQSIRSPE YDNWNLNGDL IVYHKLNDQA
IELSSMGIRV SKQDFIKQTN FANLKNDQEN NFYHQMILND QLPQTIGGGI GQSRLCMFLL
NKKHIGEVQV SVWPNEYKDE LLKKGIKLL